ID   VM3LC_MACLN             Reviewed;         205 AA.
AC   C0LZJ5;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Disintegrin-like leberagin-C;
OS   Macrovipera lebetina transmediterranea (Blunt-nosed viper) (Vipera lebetina
OS   transmediterranea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX   NCBI_TaxID=384075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-28; 135-185 AND 191-205,
RP   FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=19808093; DOI=10.1016/j.matbio.2009.09.009;
RA   Limam I., Bazaa A., Srairi-Abid N., Taboubi S., Jebali J.,
RA   Zouari-Kessentini R., Kallech-Ziri O., Mejdoub H., Hammami A., El Ayeb M.,
RA   Luis J., Marrakchi N.;
RT   "Leberagin-C, a disintegrin-like/cysteine-rich protein from Macrovipera
RT   lebetina transmediterranea venom, inhibits alphavbeta3 integrin-mediated
RT   cell adhesion.";
RL   Matrix Biol. 29:117-126(2010).
CC   -!- FUNCTION: Inhibits platelet aggregation induced by thrombin and
CC       arachidonic acid with IC(50) of 40 and 50 nM respectively (in rabbit
CC       platetelet-rich plasma). It also inhibits the adhesion of melanoma
CC       tumor cells on fibrinogen and fibronectin, by interfering with the
CC       function of alpha-V/beta-3 (ITGAV/ITGB3) and, to a lesser extent, with
CC       alpha-V/beta-6 (ITGAV/ITGB6) and alpha-5/beta-1 (ITGA5/ITGB1)
CC       integrins. {ECO:0000269|PubMed:19808093}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19808093}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=25787.02; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19808093};
CC   -!- MISCELLANEOUS: Does not interact with the alpha-2/beta-1 (ITGA2/ITGB1)
CC       integrin. Does not inhibit platelet aggregation induced by collagen or
CC       ADP (PubMed:19808093). {ECO:0000305|PubMed:19808093}.
CC   -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC       subfamily.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: The complete sequence contains a signal peptide, a propeptide
CC       domain, and a proteinase domain at the N-terminus. {ECO:0000305}.
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DR   EMBL; FJ790318; ACN88545.1; -; mRNA.
DR   AlphaFoldDB; C0LZJ5; -.
DR   SMR; C0LZJ5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..205
FT                   /note="Disintegrin-like leberagin-C"
FT                   /id="PRO_0000424622"
FT   DOMAIN          4..90
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           68..70
FT                   /note="D/ECD-tripeptide"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        7..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        18..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        62..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        69..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        101..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        113..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        151..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        163..171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        193..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   205 AA;  22634 MW;  7ABBCC2D51D44F02 CRC64;
     IVSPPVCGNE LLENGEECDC GSPANCRNPC CDAASCRLHS WVECESGECC DQCRFVTAGT
     ECRATRSECD LAGQCTGQSA DCPIDRFHRN GQPCLQNYGY CYNGKCPIMH HQCYYLFGAN
     ATVAQDACFE ENKNGIGDFY CRKQSDRLIP CAPEDVKCGR LFCEILPNTR CKHAPGDNGM
     VDPGTKCEDK KVCFNRKCVD VNTVY